Human cervical mucin, the principal glycoprotein component of the gel phase of cervical mucus, has not been structurally characterized although it regulates and is mainly responsible for the rheological properties and sperm receptivity of this mucus secretion. The proposed research seeks to characterize the oligosaccharides of human cervical mucin with respect to composition, size, structure, and distribution along the protein core. The experimental approach is to cleave the oligosaccharide-protein linkages by alkali-catalyzed beta-elimination reaction followed by purification of individual oligosaccharides. Structural analyses will utilize sequential degradations with exoglycosidases and identification of methylated alditol acetates by gas liquid chromatography/mass spectroscopy.